메뉴 건너뛰기




Volumn 17, Issue 10, 2006, Pages 4513-4525

Clathrin-dependent association of CVAK104 with endosomes and the trans-Golgi network

Author keywords

[No Author keywords available]

Indexed keywords

ADAPTOR PROTEIN; BREFELDIN A; CATHEPSIN D; CLATHRIN; GREEN FLUORESCENT PROTEIN; GUANINE NUCLEOTIDE BINDING PROTEIN; GUANOSINE 5' O (3 THIOTRIPHOSPHATE); HYDROLASE; MEMBRANE PROTEIN; PROTEIN CVAK104; PROTEIN SERINE THREONINE KINASE; PROTEIN SUBUNIT; RED FLUORESCENT PROTEIN; SOMATOMEDIN B RECEPTOR; TRANSFERRIN; UNCLASSIFIED DRUG;

EID: 33749495408     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.E06-05-0390     Document Type: Article
Times cited : (29)

References (55)
  • 1
    • 0345012707 scopus 로고
    • Structural relationships between clathrin assembly proteins from the Golgi and the plasma membrane
    • Ahle, S., Mann, A., Eichelsbacher, U., and Ungewickell, E. (1988). Structural relationships between clathrin assembly proteins from the Golgi and the plasma membrane. EMBO J. 7, 919-929.
    • (1988) EMBO J. , vol.7 , pp. 919-929
    • Ahle, S.1    Mann, A.2    Eichelsbacher, U.3    Ungewickell, E.4
  • 2
    • 0023001146 scopus 로고
    • Clathrin-coated vesicles contain two protein kinase activities. Phosphorylation of clathrin beta-light chain by casein kinase II
    • Bar-Zvi, D., and Branton, D. (1986). Clathrin-coated vesicles contain two protein kinase activities. Phosphorylation of clathrin beta-light chain by casein kinase II. J. Biol. Chem. 261, 9614-9621.
    • (1986) J. Biol. Chem. , vol.261 , pp. 9614-9621
    • Bar-Zvi, D.1    Branton, D.2
  • 3
    • 28444439900 scopus 로고    scopus 로고
    • Organelle identity and the signposts for membrane traffic
    • Behnia, R., and Munro, S. (2005). Organelle identity and the signposts for membrane traffic. Nature 438, 597-604.
    • (2005) Nature , vol.438 , pp. 597-604
    • Behnia, R.1    Munro, S.2
  • 4
    • 23844495063 scopus 로고    scopus 로고
    • N-WASP deficiency impairs EGF internalization and actin assembly at clathrin-coated pits
    • Benesch, S., Polo, S., Lai, F. P., Anderson, K. I., Stradal, T. E., Wehland, J., and Rottner, K. (2005). N-WASP deficiency impairs EGF internalization and actin assembly at clathrin-coated pits. J. Cell Sci. 118, 3103-3115.
    • (2005) J. Cell Sci. , vol.118 , pp. 3103-3115
    • Benesch, S.1    Polo, S.2    Lai, F.P.3    Anderson, K.I.4    Stradal, T.E.5    Wehland, J.6    Rottner, K.7
  • 5
    • 0022726176 scopus 로고
    • Monoclonal antibodies to soluble, human milk galactosyltransferase (lactose synthase a protein)
    • Berger, E. G., Aegerter, E., Mandel, T., and Hauri, H. P. (1986). Monoclonal antibodies to soluble, human milk galactosyltransferase (lactose synthase A protein). Carbohydr. Res. 149, 23-33.
    • (1986) Carbohydr. Res. , vol.149 , pp. 23-33
    • Berger, E.G.1    Aegerter, E.2    Mandel, T.3    Hauri, H.P.4
  • 6
    • 12144291497 scopus 로고    scopus 로고
    • Tandem MS analysis of brain clathrin-coated vesicles reveals their critical involvement in synaptic vesicle recycling
    • Blondeau, F., et al. (2004). Tandem MS analysis of brain clathrin-coated vesicles reveals their critical involvement in synaptic vesicle recycling. Proc. Natl. Acad. Sci. USA 101, 3833-3838.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 3833-3838
    • Blondeau, F.1
  • 7
    • 0022369827 scopus 로고
    • Clathrin structure characterized with monoclonal antibodies. 1. Analysis of multiple antigenic sites
    • Brodsky, F. M. (1985). Clathrin structure characterized with monoclonal antibodies. 1. Analysis of multiple antigenic sites. J. Cell Biol. 101, 2047-2054.
    • (1985) J. Cell Biol. , vol.101 , pp. 2047-2054
    • Brodsky, F.M.1
  • 9
    • 14044275140 scopus 로고    scopus 로고
    • Huntingtin-interacting protein 1 (Hip1) and Hip1-related protein (Hip1R) bind the conserved sequence of clathrin light chains and thereby influence clathrin assembly in vitro and actin distribution in vivo
    • Chen, C. Y., and Brodsky, F. M. (2005). Huntingtin-interacting protein 1 (Hip1) and Hip1-related protein (Hip1R) bind the conserved sequence of clathrin light chains and thereby influence clathrin assembly in vitro and actin distribution in vivo. J. Biol. Chem. 280, 6109-6117.
    • (2005) J. Biol. Chem. , vol.280 , pp. 6109-6117
    • Chen, C.Y.1    Brodsky, F.M.2
  • 10
    • 0024331983 scopus 로고
    • 100-kDa polypeptides in peripheral clathrin-coated vesicles are required for receptor-mediated endocytosis
    • Chin, D. J., Straubinger, R. M., Acton, S., Nathke, I., and Brodsky, F. M. (1989). 100-kDa polypeptides in peripheral clathrin-coated vesicles are required for receptor-mediated endocytosis. Proc. Natl. Acad. Sci. USA 86, 9289-9293.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 9289-9293
    • Chin, D.J.1    Straubinger, R.M.2    Acton, S.3    Nathke, I.4    Brodsky, F.M.5
  • 11
    • 0037018152 scopus 로고    scopus 로고
    • Identification of an adaptor-associated kinase, AAK1, as a regulator of clathrin-mediated endocytosis
    • Conner, S. D., and Schmid, S. L. (2002). Identification of an adaptor-associated kinase, AAK1, as a regulator of clathrin-mediated endocytosis. J. Cell Biol. 156, 921-929.
    • (2002) J. Cell Biol. , vol.156 , pp. 921-929
    • Conner, S.D.1    Schmid, S.L.2
  • 12
    • 20444365819 scopus 로고    scopus 로고
    • CVAK104 is a novel poly-L-lysine-stimulated kinase that targets the beta2-subunit of AP2
    • Conner, S. D., and Schmid, S. L. (2005). CVAK104 is a novel poly-L-lysine-stimulated kinase that targets the beta2-subunit of AP2. J. Biol. Chem. 280, 21539-21544.
    • (2005) J. Biol. Chem. , vol.280 , pp. 21539-21544
    • Conner, S.D.1    Schmid, S.L.2
  • 13
    • 0035510916 scopus 로고    scopus 로고
    • The dephosphins: Dephosphorylation by calcineurin triggers synaptic vesicle endocytosis
    • Cousin, M. A., and Robinson, P. J. (2001). The dephosphins: dephosphorylation by calcineurin triggers synaptic vesicle endocytosis. Trends Neurosci. 24, 659-665.
    • (2001) Trends Neurosci. , vol.24 , pp. 659-665
    • Cousin, M.A.1    Robinson, P.J.2
  • 14
    • 0037166331 scopus 로고    scopus 로고
    • Interaction of the cation-dependent mannose 6-phosphate receptor with GGA proteins
    • Doray, B., Bruns, K., Ghosh, P., and Kornfeld, S. (2002). Interaction of the cation-dependent mannose 6-phosphate receptor with GGA proteins. J. Biol. Chem. 277, 18477-18482.
    • (2002) J. Biol. Chem. , vol.277 , pp. 18477-18482
    • Doray, B.1    Bruns, K.2    Ghosh, P.3    Kornfeld, S.4
  • 15
    • 15544370138 scopus 로고    scopus 로고
    • Regulation of the clathrin-coated vesicle cycle by reversible phosphorylation
    • Flett, A., Semerdjieva, S., Jackson, A. P., and Smythe, E. (2005). Regulation of the clathrin-coated vesicle cycle by reversible phosphorylation. Biochem. Soc. Symp. 65-70.
    • (2005) Biochem. Soc. Symp. , pp. 65-70
    • Flett, A.1    Semerdjieva, S.2    Jackson, A.P.3    Smythe, E.4
  • 17
    • 0037336348 scopus 로고    scopus 로고
    • Mannose 6-phosphate receptors: New twists in the tale
    • Ghosh, P., Dahms, N. M., and Kornfeld, S. (2003). Mannose 6-phosphate receptors: new twists in the tale. Nat. Rev. Mol. Cell Biol. 4, 202-212.
    • (2003) Nat. Rev. Mol. Cell Biol. , vol.4 , pp. 202-212
    • Ghosh, P.1    Dahms, N.M.2    Kornfeld, S.3
  • 18
    • 0037416130 scopus 로고    scopus 로고
    • AP-1 binding to sorting signals and release from clathrin-coated vesicles is regulated by phosphorylation
    • Ghosh, P., and Kornfeld, S. (2003). AP-1 binding to sorting signals and release from clathrin-coated vesicles is regulated by phosphorylation. J. Cell Biol. 160, 699-708.
    • (2003) J. Cell Biol. , vol.160 , pp. 699-708
    • Ghosh, P.1    Kornfeld, S.2
  • 20
    • 0033978513 scopus 로고    scopus 로고
    • Role of cyclin G-associated kinase in uncoating clathrin-coated vesicles from non-neuronal cells
    • Greener, T., Zhao, X., Nojima, H., Eisenberg, E., and Greene, L. E. (2000). Role of cyclin G-associated kinase in uncoating clathrin-coated vesicles from non-neuronal cells. J. Biol. Chem. 275, 1365-1370.
    • (2000) J. Biol. Chem. , vol.275 , pp. 1365-1370
    • Greener, T.1    Zhao, X.2    Nojima, H.3    Eisenberg, E.4    Greene, L.E.5
  • 21
    • 0037351330 scopus 로고    scopus 로고
    • Changing directions: Clathrin-mediated transport between the Golgi and endosomes
    • Hinners, I., and Tooze, S. A. (2003). Changing directions: clathrin-mediated transport between the Golgi and endosomes. J. Cell Sci. 116, 763-771.
    • (2003) J. Cell Sci. , vol.116 , pp. 763-771
    • Hinners, I.1    Tooze, S.A.2
  • 22
    • 0242413645 scopus 로고    scopus 로고
    • Effect of clathrin heavy chain- and alpha-adaptin-specific small inhibitory RNAs on endocytic accessory proteins and receptor trafficking in HeLa cells
    • Hinrichsen, L., Harborth, J., Andrees, L., Weber, K., and Ungewickell, E. J. (2003). Effect of clathrin heavy chain- and alpha-adaptin-specific small inhibitory RNAs on endocytic accessory proteins and receptor trafficking in HeLa cells. J. Biol. Chem. 278, 45160-45170.
    • (2003) J. Biol. Chem. , vol.278 , pp. 45160-45170
    • Hinrichsen, L.1    Harborth, J.2    Andrees, L.3    Weber, K.4    Ungewickell, E.J.5
  • 24
    • 50549168907 scopus 로고
    • Measurement of protein-binding phenomena by gel filtration
    • Hummel, J. P., and Dreyer, W. J. (1962). Measurement of protein-binding phenomena by gel filtration. Biochim. Biophys. Acta 63, 530-532.
    • (1962) Biochim. Biophys. Acta , vol.63 , pp. 530-532
    • Hummel, J.P.1    Dreyer, W.J.2
  • 25
    • 27744520682 scopus 로고    scopus 로고
    • Rab proteins, connecting transport and vesicle fusion
    • Jordens, I., Marsman, M., Kuijl, C., and Neefjes, J. (2005). Rab proteins, connecting transport and vesicle fusion. Traffic 6, 1070-1077.
    • (2005) Traffic , vol.6 , pp. 1070-1077
    • Jordens, I.1    Marsman, M.2    Kuijl, C.3    Neefjes, J.4
  • 27
    • 0026637316 scopus 로고
    • Structure and function of the mannose 6-phosphate/ insulinlike growth factor II receptors
    • Kornfeld, S. (1992). Structure and function of the mannose 6-phosphate/ insulinlike growth factor II receptors. Annu. Rev. Biochem. 61, 307-330.
    • (1992) Annu. Rev. Biochem. , vol.61 , pp. 307-330
    • Kornfeld, S.1
  • 28
    • 0042067953 scopus 로고    scopus 로고
    • Kinases in clathrin-mediated endocytosis
    • Korolchuk, V., and Banting, G. (2003). Kinases in clathrin-mediated endocytosis. Biochem. Soc. Trans. 31, 857-860.
    • (2003) Biochem. Soc. Trans. , vol.31 , pp. 857-860
    • Korolchuk, V.1    Banting, G.2
  • 29
    • 0036704540 scopus 로고    scopus 로고
    • Clathrin-protein interactions
    • Lafer, E. M. (2002). Clathrin-protein interactions. Traffic 3, 513-520.
    • (2002) Traffic , vol.3 , pp. 513-520
    • Lafer, E.M.1
  • 30
    • 0032491411 scopus 로고    scopus 로고
    • The mammalian AP-3 adaptor-like complex mediates the intracellular transport of lysosomal membrane glycoproteins
    • Le Borgne, R., Alconada, A., Bauer, U., and Hoflack, B. (1998). The mammalian AP-3 adaptor-like complex mediates the intracellular transport of lysosomal membrane glycoproteins. J. Biol. Chem. 273, 29451-29461.
    • (1998) J. Biol. Chem. , vol.273 , pp. 29451-29461
    • Le Borgne, R.1    Alconada, A.2    Bauer, U.3    Hoflack, B.4
  • 31
    • 14044265129 scopus 로고    scopus 로고
    • Huntingtin interacting protein 1 (HIP1) regulates clathrin assembly through direct binding to the regulatory region of the clathrin light chain
    • Legendre-Guillemin, V., Metzler, M., Lemaire, J. F., Philie, J., Gan, L., Hayden, M. R., and McPherson, P. S. (2005). Huntingtin interacting protein 1 (HIP1) regulates clathrin assembly through direct binding to the regulatory region of the clathrin light chain. J. Biol. Chem. 280, 6101-6108.
    • (2005) J. Biol. Chem. , vol.280 , pp. 6101-6108
    • Legendre-Guillemin, V.1    Metzler, M.2    Lemaire, J.F.3    Philie, J.4    Gan, L.5    Hayden, M.R.6    McPherson, P.S.7
  • 32
    • 0026709661 scopus 로고
    • Clathrin-associated proteins of bovine brain coated vesicles. An analysis of their number and assembly-promoting activity
    • Lindner, R., and Ungewickell, E. (1992). Clathrin-associated proteins of bovine brain coated vesicles. An analysis of their number and assembly-promoting activity. J. Biol. Chem. 267, 16567-16573.
    • (1992) J. Biol. Chem. , vol.267 , pp. 16567-16573
    • Lindner, R.1    Ungewickell, E.2
  • 33
    • 0024361787 scopus 로고
    • Mutations in the cytoplasmic domain of the 275 kD mannose 6-phosphate receptor differentially alter lysosomal enzyme sorting and endocytosis
    • Lobel, P., Fujimoto, K., Ye, R. D., Griffiths, G., and Kornfeld, S. (1989). Mutations in the cytoplasmic domain of the 275 kD mannose 6-phosphate receptor differentially alter lysosomal enzyme sorting and endocytosis. Cell 57, 787-796.
    • (1989) Cell , vol.57 , pp. 787-796
    • Lobel, P.1    Fujimoto, K.2    Ye, R.D.3    Griffiths, G.4    Kornfeld, S.5
  • 34
    • 23844552808 scopus 로고    scopus 로고
    • Structure and function of the Lowe syndrome protein OCRL1
    • Lowe, M. (2005). Structure and function of the Lowe syndrome protein OCRL1. Traffic 6, 711-719.
    • (2005) Traffic , vol.6 , pp. 711-719
    • Lowe, M.1
  • 35
    • 0032538927 scopus 로고    scopus 로고
    • Direct pathway from early/recycling endosomes to the Golgi apparatus revealed through the study of shiga toxin B-fragment transport
    • Mallard, F., Antony, C., Tenza, D., Salamero, J., Goud, B., and Johannes, L. (1998). Direct pathway from early/recycling endosomes to the Golgi apparatus revealed through the study of shiga toxin B-fragment transport. J. Cell Biol. 143, 973-990.
    • (1998) J. Cell Biol. , vol.143 , pp. 973-990
    • Mallard, F.1    Antony, C.2    Tenza, D.3    Salamero, J.4    Goud, B.5    Johannes, L.6
  • 37
    • 0035691925 scopus 로고    scopus 로고
    • Mu 1A deficiency induces a profound increase in MPR300/IGF-II receptor internalization rate
    • Meyer, C., Eskelinen, E. L., Guruprasad, M. R., von Figura, K., and Schu, P. (2001). Mu 1A deficiency induces a profound increase in MPR300/IGF-II receptor internalization rate. J. Cell Sci. 114, 4469-4476.
    • (2001) J. Cell Sci. , vol.114 , pp. 4469-4476
    • Meyer, C.1    Eskelinen, E.L.2    Guruprasad, M.R.3    Von Figura, K.4    Schu, P.5
  • 38
    • 0034657033 scopus 로고    scopus 로고
    • mu1A-adaptin-deficient mice: Lethality, loss of AP-1 binding and rerouting of mannose 6-phosphate receptors
    • Meyer, C., Zizioli, D., Lausmann, S., Eskelinen, E. L., Hamann, J., Saftig, P., von Figura, K., and Schu, P. (2000). mu1A-adaptin-deficient mice: lethality, loss of AP-1 binding and rerouting of mannose 6-phosphate receptors. EMBO J. 19, 2193-2203.
    • (2000) EMBO J. , vol.19 , pp. 2193-2203
    • Meyer, C.1    Zizioli, D.2    Lausmann, S.3    Eskelinen, E.L.4    Hamann, J.5    Saftig, P.6    Von Figura, K.7    Schu, P.8
  • 39
    • 27744510147 scopus 로고    scopus 로고
    • Effect of clathrin assembly lymphoid myeloid leukemia protein depletion on clathrin coat formation
    • Meyerholz, A., Hinrichsen, L., Groos, S., Esk, P. C., Brandes, G., and Ungewickell, E. J. (2005). Effect of clathrin assembly lymphoid myeloid leukemia protein depletion on clathrin coat formation. Traffic 6, 1225-1234.
    • (2005) Traffic , vol.6 , pp. 1225-1234
    • Meyerholz, A.1    Hinrichsen, L.2    Groos, S.3    Esk, P.C.4    Brandes, G.5    Ungewickell, E.J.6
  • 40
    • 0032572560 scopus 로고    scopus 로고
    • ADP-Ribosylation factor 1 (ARF1) regulates recruitment of the AP-3 adaptor complex to membranes
    • Ooi, C. E., Dell'Angelica, E. C., and Bonifacino, J. S. (1998). ADP-Ribosylation factor 1 (ARF1) regulates recruitment of the AP-3 adaptor complex to membranes. J. Cell Biol. 142, 391-402.
    • (1998) J. Cell Biol. , vol.142 , pp. 391-402
    • Ooi, C.E.1    Dell'Angelica, E.C.2    Bonifacino, J.S.3
  • 41
    • 33745764302 scopus 로고    scopus 로고
    • Ultrastructure of long-range transport carriers moving from the trans-Golgi network to peripheral endosomes
    • Polishchuk, R. S., Pietro, E. S., Pentima, A. D., Tete, S., and Bonifacino, J. S. (2006). Ultrastructure of long-range transport carriers moving from the trans-Golgi network to peripheral endosomes. Traffic 7(8), 1092-1103.
    • (2006) Traffic , vol.7 , Issue.8 , pp. 1092-1103
    • Polishchuk, R.S.1    Pietro, E.S.2    Pentima, A.D.3    Tete, S.4    Bonifacino, J.S.5
  • 46
    • 0037815490 scopus 로고    scopus 로고
    • Molecular and functional characterization of clathrin- and AP-2-binding determinants within a disordered domain of auxilin
    • Scheele, U., Alves, J., Frank, R., Duwel, M., Kalthoff, C., and Ungewickell, E. (2003). Molecular and functional characterization of clathrin- and AP-2-binding determinants within a disordered domain of auxilin. J. Biol. Chem. 278, 25357-25368.
    • (2003) J. Biol. Chem. , vol.278 , pp. 25357-25368
    • Scheele, U.1    Alves, J.2    Frank, R.3    Duwel, M.4    Kalthoff, C.5    Ungewickell, E.6
  • 47
    • 0035965299 scopus 로고    scopus 로고
    • Multiple interactions of auxilin 1 with clathrin and the AP-2 adaptor complex
    • Scheele, U., Kalthoff, C., and Ungewickell, E. (2001). Multiple interactions of auxilin 1 with clathrin and the AP-2 adaptor complex. J. Biol. Chem. 276, 36131-36138.
    • (2001) J. Biol. Chem. , vol.276 , pp. 36131-36138
    • Scheele, U.1    Kalthoff, C.2    Ungewickell, E.3
  • 48
    • 0029584896 scopus 로고
    • A clathrin-binding site in the hinge of the beta 2 chain of mammalian AP-2 complexes
    • Shih, W., Gallusser, A., and Kirchhausen, T. (1995). A clathrin-binding site in the hinge of the beta 2 chain of mammalian AP-2 complexes. J. Biol. Chem. 270, 31083-31090.
    • (1995) J. Biol. Chem. , vol.270 , pp. 31083-31090
    • Shih, W.1    Gallusser, A.2    Kirchhausen, T.3
  • 49
    • 0027155088 scopus 로고
    • The binding of AP-1 clathrin adaptor particles to Golgi membranes requires ADP-ribosylation factor, a small GTP-binding protein
    • Stamnes, M. A., and Rothman, J. E. (1993). The binding of AP-1 clathrin adaptor particles to Golgi membranes requires ADP-ribosylation factor, a small GTP-binding protein. Cell 73, 999-1005.
    • (1993) Cell , vol.73 , pp. 999-1005
    • Stamnes, M.A.1    Rothman, J.E.2
  • 50
    • 0027423161 scopus 로고
    • Biochemical dissection of AP-1 recruitment onto Golgi membranes
    • Traub, L. M., Ostrom, J. A., and Kornfeld, S. (1993). Biochemical dissection of AP-1 recruitment onto Golgi membranes. J. Cell Biol. 123, 561-573.
    • (1993) J. Cell Biol. , vol.123 , pp. 561-573
    • Traub, L.M.1    Ostrom, J.A.2    Kornfeld, S.3
  • 51
    • 4544273742 scopus 로고    scopus 로고
    • The inositol polyphosphate 5-phosphatase Ocr1 associates with endosomes that are partially coated with clathrin
    • Ungewickell, A., Ward, M. E., Ungewickell, E., and Majerus, P. W. (2004). The inositol polyphosphate 5-phosphatase Ocr1 associates with endosomes that are partially coated with clathrin. Proc. Natl. Acad. Sci. USA 101, 13501-13506.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 13501-13506
    • Ungewickell, A.1    Ward, M.E.2    Ungewickell, E.3    Majerus, P.W.4
  • 52
    • 0036199384 scopus 로고    scopus 로고
    • The yeast clathrin adaptor protein complex 1 is required for the efficient retention of a subset of late Golgi membrane proteins
    • Valdivia, R. H., Baggott, D., Chuang, J. S., and Schekman, R. W. (2002). The yeast clathrin adaptor protein complex 1 is required for the efficient retention of a subset of late Golgi membrane proteins. Dev. Cell 2, 283-294.
    • (2002) Dev. Cell , vol.2 , pp. 283-294
    • Valdivia, R.H.1    Baggott, D.2    Chuang, J.S.3    Schekman, R.W.4
  • 53
    • 0037240484 scopus 로고    scopus 로고
    • Visualization of TGN to endosome trafficking through fluorescently labeled MPR and AP-1 in living cells
    • Waguri, S., Dewitte, F., Le Borgne, R., Rouille, Y., Uchiyama, Y., Dubremetz, J. F., and Hoflack, B. (2003). Visualization of TGN to endosome trafficking through fluorescently labeled MPR and AP-1 in living cells. Mol. Biol. Cell 14, 142-155.
    • (2003) Mol. Biol. Cell , vol.14 , pp. 142-155
    • Waguri, S.1    Dewitte, F.2    Le Borgne, R.3    Rouille, Y.4    Uchiyama, Y.5    Dubremetz, J.F.6    Hoflack, B.7
  • 54
    • 0028986797 scopus 로고
    • The appendage domain of alpha-adaptin is a high affinity binding site for dynamin
    • Wang, L. H., Sudhof, T. C, and Anderson, R. G. (1995). The appendage domain of alpha-adaptin is a high affinity binding site for dynamin. J. Biol. Chem. 270, 10079-10083.
    • (1995) J. Biol. Chem. , vol.270 , pp. 10079-10083
    • Wang, L.H.1    Sudhof, T.C.2    Anderson, R.G.3
  • 55
    • 0021092725 scopus 로고
    • Clathrin heavy chain, light chain interactions
    • Winkler, F. K., and Stanley, K. K. (1983). Clathrin heavy chain, light chain interactions. EMBO J. 2, 1393-1400.
    • (1983) EMBO J. , vol.2 , pp. 1393-1400
    • Winkler, F.K.1    Stanley, K.K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.